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Conserved domains on  [gi|2201770915|ref|XP_046786606|]
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protein phosphatase 1 regulatory inhibitor subunit 16B isoform X1 [Gallus gallus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-320 7.76e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 7.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  20 LERLRAAQKRRAQQLKKWAQYEKEMQHKKRKHEKKRNAVNRKKVSFEASVALLEASLRNDLEEVCYLLKSNISPDLCNED 99
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYdlcedeptl 179
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 180 dvietcmayqgitqekineMRAA----PEQVMIcdihdILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLD 255
Cdd:COG0666   158 -------------------HLAAangnLEIVKL-----LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201770915 256 VKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSLDEMPIDLCEEEEFKVLLLELKHKHDVI 320
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-320 7.76e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 7.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  20 LERLRAAQKRRAQQLKKWAQYEKEMQHKKRKHEKKRNAVNRKKVSFEASVALLEASLRNDLEEVCYLLKSNISPDLCNED 99
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYdlcedeptl 179
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 180 dvietcmayqgitqekineMRAA----PEQVMIcdihdILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLD 255
Cdd:COG0666   158 -------------------HLAAangnLEIVKL-----LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201770915 256 VKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSLDEMPIDLCEEEEFKVLLLELKHKHDVI 320
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-163 5.64e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 5.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  71 LLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHgANVNAKDNElWTPLHAAATCGHINLVK 150
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2201770915 151 ILIQHGADLLAVN 163
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-300 5.82e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSNI---SPDLCnedGLTALHQC-CIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAAT--C 143
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGAdvnAPERC---GFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 144 GHINLVKILIQHGADLLAVNADGNMPYD--LCEDEPTLDVIETCMAYQGITQEKINEMRAAPEQvmICD--------IHD 213
Cdd:PHA03095  130 INPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHH--HLQsfkprariVRE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 214 ILATGQDLNRTDAQGATLLHIAAANGYLHAAEV--LLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSART 291
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287


                  ....*....
gi 2201770915 292 SLDEMPIDL 300
Cdd:PHA03095  288 SDGNTPLSL 296
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 70-169 2.84e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSniSPDLCNE-------DGLTALHQCCIDNYEEIVKLLLSHGANVNA-----------KDN 131
Cdd:cd22192    54 ALHVAALYDNLEAAVVLMEA--APELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKN 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2201770915 132 ELW---TPLHAAATCGHINLVKILIQHGADLLAVNADGNMP 169
Cdd:cd22192   132 LIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 99-128 1.57e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.57e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2201770915   99 DGLTALHQCCIDNYEEIVKLLLSHGANVNA 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 100-177 1.68e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDN----------------ELwtPLHAAATCGHINLVKILIQHGADLLAVN 163
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyhgES--PLNAAACLGSPSIVALLSEDPADILTAD 205

                          90
                  ....*....|....
gi 2201770915 164 ADGNMPYDLCEDEP 177
Cdd:TIGR00870 206 SLGNTLLHLLVMEN 219
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-320 7.76e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 7.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  20 LERLRAAQKRRAQQLKKWAQYEKEMQHKKRKHEKKRNAVNRKKVSFEASVALLEASLRNDLEEVCYLLKSNISPDLCNED 99
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYdlcedeptl 179
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 180 dvietcmayqgitqekineMRAA----PEQVMIcdihdILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLD 255
Cdd:COG0666   158 -------------------HLAAangnLEIVKL-----LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201770915 256 VKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSLDEMPIDLCEEEEFKVLLLELKHKHDVI 320
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-236 3.61e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 3.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 149
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 150 KILIQHGADLLAVNADGNMPYDLCEDEPTLDVIETCMAYQGITQEKINEMRAAPEQVMICDIHDILATGQDLNRTDAQGA 229
Cdd:COG0666   203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                  ....*..
gi 2201770915 230 TLLHIAA 236
Cdd:COG0666   283 LDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-163 5.64e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 5.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  71 LLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHgANVNAKDNElWTPLHAAATCGHINLVK 150
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2201770915 151 ILIQHGADLLAVN 163
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-300 5.82e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSNI---SPDLCnedGLTALHQC-CIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAAT--C 143
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGAdvnAPERC---GFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 144 GHINLVKILIQHGADLLAVNADGNMPYD--LCEDEPTLDVIETCMAYQGITQEKINEMRAAPEQvmICD--------IHD 213
Cdd:PHA03095  130 INPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHH--HLQsfkprariVRE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 214 ILATGQDLNRTDAQGATLLHIAAANGYLHAAEV--LLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSART 291
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287


                  ....*....
gi 2201770915 292 SLDEMPIDL 300
Cdd:PHA03095  288 SDGNTPLSL 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-289 2.70e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.33  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  83 VCYLLKSNISPDLCNEDGLTALHQCCIDNYE-----EIVKLLLSHGANVNAKDNELWTPLHAAATC--GHINLVKILIQH 155
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 156 GADLLAVNADGNMP--YDLCEDEPTLDVIETcMAYQGItqeKINEmraapeqvmICDIHDILATGQDLNRTDAQGATLLH 233
Cdd:PHA03100  131 GANVNIKNSDGENLlhLYLESNKIDLKILKL-LIDKGV---DINA---------KNRVNYLLSYGVPINIKDVYGFTPLH 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201770915 234 IAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSA 289
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-258 7.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 7.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 104 LHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHgadllavnADGNMpydlcedeptldvie 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--------ADVNL--------------- 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201770915 184 tcmayqgitqekinemraapeqvmicdihdilatgqdlnrtDAQGATLLHIAAANGYLHAAEVLLDQGASLDVKD 258
Cdd:pfam12796  58 -----------------------------------------KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 69-286 2.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  69 VALLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINL 148
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 149 VKILIQHGADLLAV-NADGNMPYDLCEDEPTLDVIETCMAYQGITqekinemraapeqvmicdihdilatgqDLNRTDAq 227
Cdd:PHA02875   84 VEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADP---------------------------DIPNTDK- 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2201770915 228 gATLLHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGAS 286
Cdd:PHA02875  136 -FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 8-255 5.10e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 5.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915   8 LTELQLLDKVPTLERLRAAQKRRAQQLKKWAQYEKEMQHKKRKHEKKRNAVNRKKVSFEASVaLLEASLRND--LEEvcy 85
Cdd:PLN03192  468 LSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNL-LTVASTGNAalLEE--- 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  86 LLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILiQHGADLLAVNAD 165
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAA 622

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 166 GNMpydLCedeptldvietcmayqgiTQEKINEMRAAPEqvmicdihdILATGQDLNRTDAQGATLLHIAAANGYLHAAE 245
Cdd:PLN03192  623 GDL---LC------------------TAAKRNDLTAMKE---------LLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672

                         250
                  ....*....|
gi 2201770915 246 VLLDQGASLD 255
Cdd:PLN03192  673 LLIMNGADVD 682
Ank_4 pfam13637
Ankyrin repeats (many copies);
100-153 1.39e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 1.39e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILI 153
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 71-310 3.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  71 LLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHI---- 146
Cdd:PHA03100    6 VLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdv 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 147 -NLVKILIQHGADLLAVNADGNMPYDLCedeptldvIETCMAYQGItqekinemraapeqvmicdIHDILATGQDLNRTD 225
Cdd:PHA03100   86 kEIVKLLLEYGANVNAPDNNGITPLLYA--------ISKKSNSYSI-------------------VEYLLDNGANVNIKN 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 226 AQGATLLHIAAANGY--LHAAEVLLDQGA----------------SLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASL 287
Cdd:PHA03100  139 SDGENLLHLYLESNKidLKILKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218

                         250       260
                  ....*....|....*....|....*..
gi 2201770915 288 SARTSLDEMP----IDLCEEEEFKVLL 310
Cdd:PHA03100  219 NLVNKYGDTPlhiaILNNNKEIFKLLL 245
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-290 4.12e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 4.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 114 EIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAvnadgnMPYDLCEDEPTLDVIETCMAYQGITQ 193
Cdd:PHA02874   49 KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIPCIEKDMIKTILDCGIDVNIKDA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 194 EKINEMRAAPEQVMICDIHDILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQ 273
Cdd:PHA02874  123 ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202

                         170
                  ....*....|....*..
gi 2201770915 274 MQMAELLVSHGASLSAR 290
Cdd:PHA02874  203 YACIKLLIDHGNHIMNK 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-290 5.39e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.39e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201770915 214 ILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQgASLDVKDwDGWEPLHAAAFWGQMQMAELLVSHGASLSAR 290
Cdd:pfam12796  16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-322 8.20e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 8.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 113 EEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNAdgNMPYdlcedePTLDVIETcMAYQGIT 192
Cdd:PHA02874   15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINT--KIPH------PLLTAIKI-GAHDIIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 193 QEKINEMRAAPEQVMICD---IHDILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAA 269
Cdd:PHA02874   86 LLIDNGVDTSILPIPCIEkdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2201770915 270 FWGQMQMAELLVSHGASLSARTSLDEMPI-DLCEEEEFKVLLLELKHKHDVIMK 322
Cdd:PHA02874  166 KHNFFDIIKLLLEKGAYANVKDNNGESPLhNAAEYGDYACIKLLIDHGNHIMNK 219
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 108-299 3.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 108 CIDNyeEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYDLCEDEPTLDVIETCM- 186
Cdd:PHA02874  101 CIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLe 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 187 --AYQGITQEKINE-MRAAPEQVMICDIHDILATGQDLNRTDAQGATLLHIAAAngYLHAAEVLLDQGASLDVKDWDGWE 263
Cdd:PHA02874  179 kgAYANVKDNNGESpLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGST 256

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2201770915 264 PLH-AAAFWGQMQMAELLVSHGASLSARTSLDEMPID 299
Cdd:PHA02874  257 PLHhAINPPCDIDIIDILLYHKADISIKDNKGENPID 293
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-205 7.87e-11

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 7.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 116 VKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYDLCEDEPTLDVIETCMAYQGITQEk 195
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE- 176

                          90
                  ....*....|
gi 2201770915 196 iNEMRAAPEQ 205
Cdd:PTZ00322  177 -LGANAKPDS 185
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-268 2.84e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  41 EKEMQHKKRKHEKKRNAVNRKKVSFeasvaLLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLL 120
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTF-----LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 121 SHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPydlcedeptldvIETCMAYQgitqekinemR 200
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP------------LHNAIIHN----------R 235

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201770915 201 AAPEqvmicdihdILATGQDLNRTDAQGATLLHIAAANG-YLHAAEVLLDQGASLDVKDWDGWEPLHAA 268
Cdd:PHA02874  236 SAIE---------LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
232-283 6.10e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 6.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2201770915 232 LHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSH 283
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 115-298 7.70e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 7.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 115 IVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYDLCEDEPTLDVI------------ 182
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrsnink 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 183 --------------ETCMAY--QGITQEKINEMRAAPEQVMICD------IHDILATGQDLNRTDAQGATLLHIAAANGY 240
Cdd:PHA02876  240 ndlsllkairnedlETSLLLydAGFSVNSIDDCKNTPLHHASQApslsrlVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 241 -LHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQ-MAELLVSHGASLSARTSLDEMPI 298
Cdd:PHA02876  320 dTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPI 379
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-158 1.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  78 NDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGA 157
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  .
gi 2201770915 158 D 158
Cdd:PHA03100  250 S 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 104-326 1.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 104 LHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAatCGHIN------LVKILIQH--GADLLAVNADGN-------- 167
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII--CKEPNklgmkeMIRSINKCsvFYTLVAIKDAFNnrnveifk 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 168 -MPYDLCEDEPTLDVIETC-MAYQGITQEKINEMraapeqvmicdihdILATGQDLNRTDA-QGATLLHIAAANGYLHAA 244
Cdd:PHA02878  119 iILTNRYKNIQTIDLVYIDkKSKDDIIEAEITKL--------------LLSYGADINMKDRhKGNTALHYATENKDQRLT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 245 EVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSLDEMP--IDLCEEEEFKVLLLELKHKHDVIMK 322
Cdd:PHA02878  185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPlhISVGYCKDYDILKLLLEHGVDVNAK 264


                  ....
gi 2201770915 323 SQMR 326
Cdd:PHA02878  265 SYIL 268
Ank_5 pfam13857
Ankyrin repeats (many copies);
119-173 4.97e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 4.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201770915 119 LLSHG-ANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYDLC 173
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
230-281 7.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 7.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2201770915 230 TLLHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLV 281
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-287 1.22e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 110 DNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKI---LIQHGADllaVNAdgnmpYDLCEDEPtldvIETCM 186
Cdd:PHA03095   24 NVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGAD---VNA-----PERCGFTP----LHLYL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 187 AYqgitQEKINEMRaapeqVMIcdihdilATGQDLNRTDAQGATLLHIAAANGYLHA--AEVLLDQGASLDVKDWDGWEP 264
Cdd:PHA03095   92 YN----ATTLDVIK-----LLI-------KAGADVNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTP 155

                         170       180
                  ....*....|....*....|...
gi 2201770915 265 LHAaafwgqmqmaeLLVSHGASL 287
Cdd:PHA03095  156 LAV-----------LLKSRNANV 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 70-133 1.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 1.98e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNEL 133
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-298 2.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  86 LLKSNISPDLCNEDGLTALHQCCIDNYE-EIVKLLLSHGANVNAKDNELWTPLHAAATCG-HINLVKILIQHGADllaVN 163
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGAN---VN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 164 ADgnmpyDLCEDEPTldvietcmayqgitqekinEMRAAPEQVMIcdIHDILATGQDLNRTDAQGATLLHIA--AANGYL 241
Cdd:PHA02876  370 AR-----DYCDKTPI-------------------HYAAVRNNVVI--INTLLDYGADIEALSQKIGTALHFAlcGTNPYM 423

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2201770915 242 hAAEVLLDQGASLDVKDWDGWEPLHAAAFWG-QMQMAELLVSHGASLSARTSLDEMPI 298
Cdd:PHA02876  424 -SVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02798 PHA02798
ankyrin-like protein; Provisional
 114-266 5.22e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.61  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 114 EIVKLLLSHGANVNAKDNELWTPLHAAATC-----GHINLVKILIQHGADLLAVNADGNMPydLCedeptldvietCMAY 188
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETP--LY-----------CLLS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 189 QGITQEKINemraapeqvmicdIHDILATGQDLNRTDAQGATLLHIAAANGY---LHAAEVLLDQGASLDV-KDWDGWEP 264
Cdd:PHA02798  119 NGYINNLEI-------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDT 185


                  ..
gi 2201770915 265 LH 266
Cdd:PHA02798  186 LH 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-287 6.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  58 VNRKKVSFEASVALLeASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCC-IDNYEEIVKLLLSHGANVNAKDNELWTP 136
Cdd:PHA02876  300 VNAKNIKGETPLYLM-AKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTP 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 137 LHAAATCGHINLVKILIQHGADLLAVNAD--GNMPYDLCEDEPTLDVietcmayqgitqekinemraapeqvmicdiHDI 214
Cdd:PHA02876  379 IHYAAVRNNVVIINTLLDYGADIEALSQKigTALHFALCGTNPYMSV------------------------------KTL 428

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201770915 215 LATGQDLNRTDAQGATLLHIAAANG-YLHAAEVLLDQGASLDVKDWDGWEPLHAAAfwGQMQMAELLVSHGASL 287
Cdd:PHA02876  429 IDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 214-296 1.00e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 214 ILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGA---SLSAR 290
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfELGAN 180


                  ....*.
gi 2201770915 291 TSLDEM 296
Cdd:PTZ00322  181 AKPDSF 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 70-169 2.84e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSniSPDLCNE-------DGLTALHQCCIDNYEEIVKLLLSHGANVNA-----------KDN 131
Cdd:cd22192    54 ALHVAALYDNLEAAVVLMEA--APELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKN 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2201770915 132 ELW---TPLHAAATCGHINLVKILIQHGADLLAVNADGNMP 169
Cdd:cd22192   132 LIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-131 3.72e-07

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.51  E-value: 3.72e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2201770915  99 DGLTALHQCCID-NYEEIVKLLLSHGANVNAKDN 131
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 114-268 5.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 114 EIVKLLLSHGANVNAKD-NELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMPYDLCEDEPTLDVIETCMAYQGIT 192
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 193 QEKiNEMRAAPEQVMICDIHDI------LATGQDLN-RTDAQGATLLHIAaangyLHAAEV---LLDQGASLDVKDWDGW 262
Cdd:PHA02878  228 DAR-DKCGNTPLHISVGYCKDYdilkllLEHGVDVNaKSYILGLTALHSS-----IKSERKlklLLEYGADINSLNSYKL 301


                  ....*.
gi 2201770915 263 EPLHAA 268
Cdd:PHA02878  302 TPLSSA 307
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 71-282 1.58e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  71 LLEASLRNDLEEVCYLLKSNiSPDLCNEDGL--TALHQCCI-DNYEEIVKLLLSHGANVN-AKDNELW---TPLHAAATC 143
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCP-SCDLFQRGALgeTALHVAALyDNLEAAVVLMEAAPELVNePMTSDLYqgeTALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 144 GHINLVKILIQHGADLLAVNADGNM----PYDLCE-DEPTLdVIETCMAYQGITQEKINEmraapeqvmicdihdilatG 218
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGTFfrpgPKNLIYyGEHPL-SFAACVGNEEIVRLLIEH-------------------G 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201770915 219 QDLNRTDAQGATLLHIAA--ANGYL--HAAEVLL-----DQGASLD-VKDWDGWEPLHAAAFWGQMQMAELLVS 282
Cdd:cd22192   160 ADIRAQDSLGNTVLHILVlqPNKTFacQMYDLILsydkeDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 236-315 2.60e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 236 AANGYLHAAEVLLDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSLDEMPIDLCEEEEFK-VLLLELK 314
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFReVVQLLSR 169


                  .
gi 2201770915 315 H 315
Cdd:PTZ00322  170 H 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-164 3.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 3.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201770915  92 SPDLCNEdglTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLH-AAATCGHINLVKILIQHGADllaVNA 164
Cdd:PHA02878  196 IPDKTNN---SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGVD---VNA 263
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 134-163 8.24e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 8.24e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2201770915 134 WTPLHAAAT-CGHINLVKILIQHGADLLAVN 163
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-169 1.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  86 LLKSNISPDLCNEDGLTALHQC---CIDnyEEIVKLLLSHGANVNAKDNEL-WTPLHAAATCGHInlVKILIQHGADLLA 161
Cdd:PHA02878  220 LLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVNAKSYILgLTALHSSIKSERK--LKLLLEYGADINS 295


                  ....*...
gi 2201770915 162 VNADGNMP 169
Cdd:PHA02878  296 LNSYKLTP 303
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 99-128 1.57e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.57e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2201770915   99 DGLTALHQCCIDNYEEIVKLLLSHGANVNA 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 134-159 1.92e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.92e-05
                           10        20
                   ....*....|....*....|....*.
gi 2201770915  134 WTPLHAAATCGHINLVKILIQHGADL 159
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
70-120 2.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2201770915  70 ALLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLL 120
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 86-187 2.42e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  86 LLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGH--INLVKILIQHGADL-LAV 162
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSV 137

                          90       100
                  ....*....|....*....|....*
gi 2201770915 163 NADGNMPYDLCEDePTLDVIETCMA 187
Cdd:PHA02946  138 DEEGCGPLLACTD-PSERVFKKIMS 161
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 211-285 2.58e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 211 IHDILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLDVKDWDG----WEPL---HAAAFWGQMQMAELLVSH 283
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGntalWNAIsakHHKIFRILYHFASISDPH 620


                  ..
gi 2201770915 284 GA 285
Cdd:PLN03192  621 AA 622
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-248 6.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 6.23e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2201770915 211 IHDILATGQDLNRTDAQGATLLHIAAANGYLHAAEVLL 248
Cdd:pfam13637  17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
90-140 7.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 7.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2201770915  90 NISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAA 140
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-169 9.79e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 9.79e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2201770915 134 WTPLHAAATCGHINLVKILIQHGADLLAVNADGNMP 169
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-268 1.07e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201770915 214 ILATGQ-DLNRTDAQGATLLHIAAANGYLHAAEVLLDQGASLDVKDWDGWEPLHAA 268
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 68-166 1.17e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  68 SVALLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHIN 147
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                          90
                  ....*....|....*....
gi 2201770915 148 LVKILIQHGADLLAVNADG 166
Cdd:PTZ00322  163 VVQLLSRHSQCHFELGANA 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 114-168 1.31e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 1.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2201770915 114 EIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNM 168
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 134-161 1.48e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.48e-04
                          10        20
                  ....*....|....*....|....*...
gi 2201770915 134 WTPLHAAATCGHINLVKILIQHGADLLA 161
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 100-177 1.68e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDN----------------ELwtPLHAAATCGHINLVKILIQHGADLLAVN 163
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyhgES--PLNAAACLGSPSIVALLSEDPADILTAD 205

                          90
                  ....*....|....
gi 2201770915 164 ADGNMPYDLCEDEP 177
Cdd:TIGR00870 206 SLGNTLLHLLVMEN 219
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-128 1.80e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 1.80e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2201770915  99 DGLTALHQCCIDNYEEIVKLLLSHGANVNA 128
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 96-170 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  96 CNEDGLTALHQCCIDNY--EEIVKLLLSHGANVNAK--DNELwTPLHAAATCG---HINLVKILIQHGADLLAVNADGNM 168
Cdd:PHA02859   47 CNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtrDNNL-SALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKN 125


                  ..
gi 2201770915 169 PY 170
Cdd:PHA02859  126 LL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 204-319 2.27e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 204 EQVMICDIHDILATGQDLNRTDAQGATLLHIaaangYLHAA--------EVLLDQGASLDVKDWDGWEPLHAAAFWGQ-M 274
Cdd:PHA03095   23 SNVTVEEVRRLLAAGADVNFRGEYGKTPLHL-----YLHYSsekvkdivRLLLEAGADVNAPERCGFTPLHLYLYNATtL 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2201770915 275 QMAELLVSHGASLSARTSLDEMPIDLC---EEEEFKVLLLELKHKHDV 319
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLHVYlsgFNINPKVIRLLLRKGADV 145
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 79-169 2.36e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.13  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  79 DLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNY--EEIVKLLLSHGANVNAKDNELWTPLHA------------AATCG 144
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildPETDN 375

                          90       100
                  ....*....|....*....|....*..
gi 2201770915 145 HINL--VKILIQHGADLLAVNADGNMP 169
Cdd:PHA02716  376 DIRLdvIQCLISLGADITAVNCLGYTP 402
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 108-301 1.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 108 CIDNYEEIVKL-----LLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVN--ADGNMPYDLCEDEPTLD 180
Cdd:PHA02876   11 CRGNCIDILSAidnydLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIYITdhKCHSTLHTICIIPNVMD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 181 VIET----C-----MAYQGI--TQEKINE--MRAAPEQVMICDIHdilatGQDLNRTdAQGATLLHIAAANGYLHAAEVL 247
Cdd:PHA02876   91 IVISltldCdiildIKYASIilNKHKLDEacIHILKEAISGNDIH-----YDKINES-IEYMKLIKERIQQDELLIAEML 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2201770915 248 LDQGASLDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSArTSLDEMPIDLC 301
Cdd:PHA02876  165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI-IALDDLSVLEC 217
PHA02946 PHA02946
ankyin-like protein; Provisional
 113-266 1.47e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 113 EEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILIQHGADLLAVNADGNMP--YDLCEDEPTLDVIETCMAYQG 190
Cdd:PHA02946   52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERINLLVQYGA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 191 ITQEKINEMRAAPeqVMICD------IHDILATGQDLNRTDAQGATLL--HIAAANGYLHAAEVLLDQGASLDVKDWDGW 262
Cdd:PHA02946  132 KINNSVDEEGCGP--LLACTdpservFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGN 209


                  ....
gi 2201770915 263 EPLH 266
Cdd:PHA02946  210 TPLH 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 260-291 1.53e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2201770915 260 DGWEPLHAAA-FWGQMQMAELLVSHGASLSART 291
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 199-293 2.88e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 199 MRAAPE---QVMICDIHdilatgqdlnrtdaQGATLLHIAAANGYLHAAEVLLDQGASL--------------DVKDWDG 261
Cdd:cd22192    71 MEAAPElvnEPMTSDLY--------------QGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYG 136

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2201770915 262 WEPLHAAAFWGQMQMAELLVSHGASLSARTSL 293
Cdd:cd22192   137 EHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-258 3.14e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 3.14e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2201770915 227 QGATLLHIAAA-NGYLHAAEVLLDQGASLDVKD 258
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 71-128 3.75e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2201770915  71 LLEASLRNDLEEVCYLLKSNISPDLCNEDGLTALHQCCIDNYEEIVKLLLSHGANVNA 128
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 99-206 3.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915  99 DGLTALHQCCIDNY---EEIVKLLLSHGANVNAKDNELWTPLHAAAT-CG-HINLVKILIQHGADLLAVNADGN---MPY 170
Cdd:PHA02859   86 NNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHMYMCnFNvRINVIKLLIDSGVSFLNKDFDNNnilYSY 165

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2201770915 171 DLCEDEptlDVIETCMAYQGITQEKINEMRAAPEQV 206
Cdd:PHA02859  166 ILFHSD---KKIFDFLTSLGIDINETNKSGYNCYDL 198
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 193-290 4.06e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 193 QEKINEM---RAAPE-------QVMICDIHDILATGqdlnrtdAQGATLLHIAAANGYLHAAEVLLDQGASLdVKD---- 258
Cdd:cd22192    13 QKRISESpllLAAKEndvqaikKLLKCPSCDLFQRG-------ALGETALHVAALYDNLEAAVVLMEAAPEL-VNEpmts 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2201770915 259 --WDGWEPLHAAAFWGQMQMAELLVSHGAS-LSAR 290
Cdd:cd22192    85 dlYQGETALHIAVVNQNLNLVRELIARGADvVSPR 119
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 100-164 5.83e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.48  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201770915 100 GLTALHQCCIDNYEEIVKLLLSHGANVNAKDN---------------ELwtPLHAAATCGHINLVKILIQHGADLLAVNA 164
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyfgEL--PLSLAACTNQEEIVRLLLENGAQPAALEA 150
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 100-155 7.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 7.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2201770915 100 GLTALHQCCIDnyEEIVKLLLSHGANVNAKDNELWTPLHAAA-TCGHINLVKILIQH 155
Cdd:PHA02878  269 GLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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